Glycation of bovine serum albumin with monosaccharides inhibits heat-induced protein aggregation

Abstract Depending upon the metal coordination capacity and the binding sites of proteins, interaction between metal and proteins leads to a number of changes in the protein molecule which may include the change in conformation, unfolding, overall charge, and aggregation in some cases. In this study, Cu(ii) and Ag(i) metal ions were selected to investigate aggregation of bovine serum albumin (BSA) molecule upon interaction by measuring the size and charge of the aggregates using nano-Zetasizer instrument. Two concentrations of metal ions were made to interact with a specific concentration of BSA and the size and zeta potential of BSA aggregates were measured from 0 min upto 18 h. The Cu(ii) and Ag(i) metal ions showed almost similar behavior in inducing the BSA aggregation and the intensity of peak corresponding to the normal-sized protein decreased with time, whereas the peak corresponding to the protein aggregate increased. However, the effect on zeta potential of the aggregates was observed to be different with both metal ions. The aggregation of protein due to interaction of different metal ions is important to study as it gives insight to the pathogenesis of many neurological disorders and would result in developing effective ways to limit their exposure.

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Dynamic Measurements of Bovine Serum Albumin Aggregation Using Small Angle Neutron Scattering

10.1101/368092 ◽

2018 ◽

Cited By ~ 1

Author(s):

James I Austerberry ◽

Daniel J Belton

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Protein Aggregation ◽

Neutron Scattering ◽

Small Angle ◽

Bovine Serum ◽

Small Angle Neutron Scattering ◽

Scattering Data ◽

Complex Nature ◽

Population Modelling

AbstractThe rapid and complex nature of protein aggregation makes the identification of aggregation mechanisms and their precursors challenging. Here we demonstrate the novel use of small-angle neutron scattering to perform dynamic real-time measurement and analysis of protein aggregation. Changes in bovine serum albumin monomer population and aggregate size are identified at several isothermal temperatures. Kratky plots indicate that the aggregation of BSA occurs through the partial unfolding of the monomer. Dual population modelling of the scattering data indicates that the protein nucleates and grows through a two stage mechanism; a rapid burst phase and a slower growth phase. Both stages are observed to follow Arrhenius behaviour between 70-80 °C.

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Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin

Biotechnology Reports ◽

10.1016/j.btre.2016.01.002 ◽

2016 ◽

Vol 9 ◽

pp. 46-52 ◽

Cited By ~ 66

Author(s):

Rui Li ◽

Zhaoliang Wu ◽

Yanji Wangb ◽

Linlin Ding ◽

Yanyan Wang

Keyword(s):

Structural Change ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Protein Aggregation ◽

Bovine Serum ◽

Foam Fractionation

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Anti-aggregation effect of Ascorbic Acid and Quercetin on aggregated Bovine Serum Albumin Induced by Dithiothreitol: Comparison of Turbidity and Soluble Protein Fraction Methods

Jurnal Kimia Sains dan Aplikasi ◽

10.14710/jksa.23.4.129-134 ◽

2020 ◽

Vol 23 (4) ◽

pp. 129-134

Author(s):

Amat Rifai ◽

Mukhammad Asy'ari ◽

Agustina L. N. Aminin

Keyword(s):

Ascorbic Acid ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Protein Aggregation ◽

Soluble Protein ◽

Bovine Serum ◽

Disulfide Bonds ◽

Protein Profile ◽

Turbidity Method ◽

Aggregation Activity

Studies on the anti-aggregation of dithiothreitol (DTT) induced - protein is generally determined by the fraction soluble (non-aggregated) protein. While the turbidity method is commonly used in studies of anti-aggregation, in which protein is induced by heat, in this study, both methods are compared in observing the anti-aggregation activity of ascorbic acid and quercetin toward bovine serum albumin induced by DTT. The DTT is a reducing agent for protein disulfide bonds and capable of inducing protein aggregation at physiological pH and temperature. The work was performed by the formation of Bovine Serum Albumin (BSA) aggregates induced by DTT under physiological conditions, which are pH 7.4 and 37°C. The aggregated protein profile was observed using the turbidity method at the end of incubation and measuring the difference of concentration between the fraction of soluble protein before and after incubation. The measurement was carried out using a spectrophotometer UV-Vis. The results indicate that both methods show similar inhibition profiles. The potential inhibition of ascorbic acid (AA) toward BSA protein aggregation induced by DTT increased along with incubation time. While quercetin shows the highest inhibition at 12 hours but decreased at 18 hours, this study reveals that both methods can observe the anti-aggregation activity of ascorbic acid and quercetin.

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Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100128122 ◽

1987 ◽

Vol 45 ◽

pp. 762-763

Author(s):

G. D. Gagne ◽

M. F. Miller

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Artificial Substrate ◽

Chemical Fixation ◽

As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

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